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Database: UniProt
Entry: M2WA66_GALSU
LinkDB: M2WA66_GALSU
Original site: M2WA66_GALSU 
ID   M2WA66_GALSU            Unreviewed;       521 AA.
AC   M2WA66;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN   ORFNames=Gasu_01510 {ECO:0000313|EMBL:EME32791.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME32791.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
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DR   EMBL; KB454484; EME32791.1; -; Genomic_DNA.
DR   RefSeq; XP_005709311.1; XM_005709254.1.
DR   AlphaFoldDB; M2WA66; -.
DR   STRING; 130081.M2WA66; -.
DR   EnsemblPlants; EME32791; EME32791; Gasu_01510.
DR   GeneID; 17091341; -.
DR   Gramene; EME32791; EME32791; Gasu_01510.
DR   KEGG; gsl:Gasu_01510; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   OMA; KNSAMVC; -.
DR   OrthoDB; 1308at2759; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR   CDD; cd00502; DHQase_I; 1.
DR   CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00214; AroD; 1.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR011342; Shikimate_DH.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   NCBIfam; TIGR01093; aroD; 1.
DR   NCBIfam; TIGR00507; aroE; 1.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000313|EMBL:EME32791.1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000313|EMBL:EME32791.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT   DOMAIN          231..310
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          361..431
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          483..513
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   521 AA;  58013 MW;  7D428FB65CA3519F CRC64;
     MSGCLLCVPI TAQYVKEAFE QIKEAQRLGA DLVELRLDLL DSTEEWEDLV KHCFVPKIAT
     CRPHWEGGNY NGSESRRLSI LSEACKLGCE YVDVELEAIT RFEKPSNCHT KLILSRHLWN
     RPFSHQELAN TYSSMLSNQA DVIKVACKID NIEQCEILFH FIAASKVPCI ALGMGEAGQI
     SRILAGRYGA FLTFASLSKG KESAPGQIEL NDCIQMYRLK SLSSSTKLYG VVGNPVAHSM
     SPAIHNLAFA SLSLDCVYCP LAVEDFGSCW KMLNEMGFMG LSVTIPHKET AKRYVDELDG
     LALKIGAINT MVKLERGWKG YNTDCLAAVS AIEDGLIAQR SSSELSHRTN SFSTQAGAKP
     LVLILGAGGA ARAIAFGLLE RSYNIYVVNR NYDRCKKLAA ELGIEAIPWE GLRRFLLEHK
     DSIDVIIQST SIGMHPNVHD TPLSFDDLQS LSKKPLVFDV VYNPVETRFL REAREVGCYV
     VSGLEMFVRQ AVYQFELWTG SKAPVEQMRQ VVLKRLKTFM E
//
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